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1p4b
From Proteopedia
Revision as of 21:34, 28 September 2014 by OCA (Talk | contribs)
1p4b is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We generated a single chain Fv fragment of an antibody (scFv) with a binding affinity of about 5 pm to a short peptide by applying rigorous directed evolution. Starting from a high affinity peptide binder, originally obtained by ribosome display from a murine library, we generated libraries of mutants with error-prone PCR and DNA shuffling and applied off-rate selection by using ribosome display. Crystallographic analysis of the scFv in its antigen-bound and free state showed that only few mutations, which do not make direct contact to the antigen, lead to a 500-fold affinity improvement over its potential germ line precursor. These results suggest that the affinity optimization of very high affinity binders is achieved by modulating existing interactions via subtle changes in the framework rather than by introducing new contacts. Off-rate selection in combination with ribosome display can evolve binders to the low picomolar affinity range even for peptide targets.
Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity.,Zahnd C, Spinelli S, Luginbuhl B, Amstutz P, Cambillau C, Pluckthun A J Biol Chem. 2004 Apr 30;279(18):18870-7. Epub 2004 Jan 30. PMID:14754898[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Zahnd C, Spinelli S, Luginbuhl B, Amstutz P, Cambillau C, Pluckthun A. Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity. J Biol Chem. 2004 Apr 30;279(18):18870-7. Epub 2004 Jan 30. PMID:14754898 doi:10.1074/jbc.M309169200
